Chondroitin sulfate 846 epitope (CS846) can be used as a marker for newly synthesized aggrecan molecules in the matrix, and its presence in synovial fluid and serum can reflect the rate of aggrecan synthesis. The reactivity of CS846 was increased in human OA samples, where increased synthesis of aggrecan was generally observed. Creative BioMart Biomarker is capable to provide our customers with superior CS846 detection service, various detection methods ensuring high sensitivity for detecting biomarkers in different samples with different concentrations.
Changes in the functional properties and disorders of articular cartilage in osteoarthritis (OA) are the result of changes in matrix macromolecular degradation, synthesis, structure and interaction. During the development of OA, changes occur not only in the degradation of matrix molecules, but also in the rate of synthesis and structure of various matrix components. These changes can represent the response of cells to joint and tissue damage and can serve as metabolic markers of tissue damage. The release of matrix macromolecular fragments and proteases following human OA or joint damage provides evidence of increased matrix turnover. Therefore, increased concentrations of fragmented type II collagen, aggrecan, cartilage oligomeric matrix protein (COMP), and bone sialoprotein (BSP) was detected in articular cartilage or synovial fluid of OA patients, accompanied by significant increase in matrix metalloproteinase 1 (MMP-1) and MMP-3 levels in synovial fluid. Aggrecan is a major component of the extracellular matrix (ECM) in cartilage and is a large proteoglycan. Aggrecan interacts with hyaluronan and link protein and forms large aggregated complexes that fill the interstices of the collagen meshwork. Aggrecan degradation is an important marker of OA, and CS846 is a marker of aggrecan synthesis. The level of CS846 is elevated in cartilage and synovial fluid of OA patients, and related to the progression of joint damage in rheumatoid arthritis (RA).
Figure 1. Structure of proteoglycan aggregates.
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